3S19
Crystal Structure of the R262L mutant of 7-cyano-7-deazaguanine reductase, QueF from Vibrio cholerae complexed with preQ0
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003674 | molecular_function | molecular_function |
A | 0005575 | cellular_component | cellular_component |
A | 0005737 | cellular_component | cytoplasm |
A | 0006400 | biological_process | tRNA modification |
A | 0008150 | biological_process | biological_process |
A | 0008616 | biological_process | queuosine biosynthetic process |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0033739 | molecular_function | preQ1 synthase activity |
A | 0046857 | molecular_function | oxidoreductase activity, acting on other nitrogenous compounds as donors, with NAD or NADP as acceptor |
B | 0003674 | molecular_function | molecular_function |
B | 0005575 | cellular_component | cellular_component |
B | 0005737 | cellular_component | cytoplasm |
B | 0006400 | biological_process | tRNA modification |
B | 0008150 | biological_process | biological_process |
B | 0008616 | biological_process | queuosine biosynthetic process |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0033739 | molecular_function | preQ1 synthase activity |
B | 0046857 | molecular_function | oxidoreductase activity, acting on other nitrogenous compounds as donors, with NAD or NADP as acceptor |
C | 0003674 | molecular_function | molecular_function |
C | 0005575 | cellular_component | cellular_component |
C | 0005737 | cellular_component | cytoplasm |
C | 0006400 | biological_process | tRNA modification |
C | 0008150 | biological_process | biological_process |
C | 0008616 | biological_process | queuosine biosynthetic process |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0033739 | molecular_function | preQ1 synthase activity |
C | 0046857 | molecular_function | oxidoreductase activity, acting on other nitrogenous compounds as donors, with NAD or NADP as acceptor |
D | 0003674 | molecular_function | molecular_function |
D | 0005575 | cellular_component | cellular_component |
D | 0005737 | cellular_component | cytoplasm |
D | 0006400 | biological_process | tRNA modification |
D | 0008150 | biological_process | biological_process |
D | 0008616 | biological_process | queuosine biosynthetic process |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0033739 | molecular_function | preQ1 synthase activity |
D | 0046857 | molecular_function | oxidoreductase activity, acting on other nitrogenous compounds as donors, with NAD or NADP as acceptor |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE PRF A 290 |
Chain | Residue |
A | TRP62 |
A | GLU234 |
A | ILE267 |
A | LEU92 |
A | ILE93 |
A | GLU94 |
A | SER95 |
A | CYS194 |
A | ASP201 |
A | PHE232 |
A | HIS233 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 291 |
Chain | Residue |
A | ALA90 |
A | ASN91 |
A | HOH665 |
D | ASN91 |
D | HOH690 |
D | HOH836 |
site_id | AC3 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE PRF B 290 |
Chain | Residue |
B | TRP62 |
B | LEU92 |
B | ILE93 |
B | GLU94 |
B | SER95 |
B | CYS194 |
B | ILE196 |
B | ASP201 |
B | PHE232 |
B | HIS233 |
B | GLU234 |
B | LEU262 |
B | ILE267 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL B 291 |
Chain | Residue |
B | THR63 |
B | TYR65 |
B | GLU82 |
B | TYR142 |
B | ARG258 |
B | ASN281 |
B | ARG283 |
site_id | AC5 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE PRF C 290 |
Chain | Residue |
C | TRP62 |
C | LEU92 |
C | ILE93 |
C | GLU94 |
C | SER95 |
C | CYS194 |
C | ILE196 |
C | ASP201 |
C | GLU231 |
C | PHE232 |
C | HIS233 |
C | GLU234 |
C | LEU262 |
C | ILE267 |
site_id | AC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL C 291 |
Chain | Residue |
C | THR63 |
C | TYR65 |
C | GLU82 |
C | TYR142 |
C | ARG258 |
C | ASN281 |
C | ARG283 |
C | HOH518 |
C | HOH897 |
site_id | AC7 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE PRF D 290 |
Chain | Residue |
D | TRP62 |
D | LEU92 |
D | ILE93 |
D | GLU94 |
D | SER95 |
D | CYS194 |
D | ILE196 |
D | ASP201 |
D | PHE232 |
D | HIS233 |
D | GLU234 |
D | ILE267 |
site_id | AC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL D 291 |
Chain | Residue |
D | THR63 |
D | TYR65 |
D | GLU82 |
D | TYR142 |
D | ARG258 |
D | ASN281 |
D | ARG283 |
D | HOH789 |
D | HOH1171 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Thioimide intermediate => ECO:0000255|HAMAP-Rule:MF_00817, ECO:0000269|Ref.3 |
Chain | Residue | Details |
A | CYS194 | |
B | CYS194 | |
C | CYS194 | |
D | CYS194 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00817 |
Chain | Residue | Details |
A | ASP201 | |
B | ASP201 | |
C | ASP201 | |
D | ASP201 |
site_id | SWS_FT_FI3 |
Number of Residues | 16 |
Details | BINDING: |
Chain | Residue | Details |
A | ILE93 | |
C | SER95 | |
C | HIS233 | |
C | LEU262 | |
D | ILE93 | |
D | SER95 | |
D | HIS233 | |
D | LEU262 | |
A | SER95 | |
A | HIS233 | |
A | LEU262 | |
B | ILE93 | |
B | SER95 | |
B | HIS233 | |
B | LEU262 | |
C | ILE93 |